1.1.1.49: glucose-6-phosphate dehydrogenase (NADP+)

This is an abbreviated version, for detailed information about glucose-6-phosphate dehydrogenase (NADP+), go to the full flat file.

Reaction

D-glucose 6-phosphate
+
NADP+
=
6-phospho-D-glucono-1,5-lactone
+
NADPH
+
H+

Synonyms

6-phosphoglucose dehydrogenase, D-glucose 6-phosphate dehydrogenase, D-glucose 6-phosphate: NADP+ oxidoreductase, D-glucose-6-phosphate: NADP+ oxidoreductase, D-glucose-6-phosphate:NADP oxidoreductase, Entner-Doudoroff enzyme, G-6-PD, G-6-PDH, G-6PD, G6PD, G6PD1, G6PD2, G6PD3, G6PD4, G6PD5, G6PD6, G6PDH, G6PDH-1, G6PDH-2, G6PDH1, G6PDH2, G6PDH3, G6PDH4, G6PDH5, G6PDH6, Glc6PDH, glucose 6-phosphate dehydrogenase, glucose 6-phosphate dehydrogenase (NADP), glucose-6-phosphate 1-dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, GPD, KlZWF1, NADP-dependent glucose 6-phophate dehydrogenase, NADP-glucose-6-phosphate dehydrogenase, PfGluPho, VEG11, Vegetative protein 11, Zwischenferment

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.49 glucose-6-phosphate dehydrogenase (NADP+)

Engineering

Engineering on EC 1.1.1.49 - glucose-6-phosphate dehydrogenase (NADP+)

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A44T
-
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T
G163D
-
mutant is markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G163S
-
mutant markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G488S
-
clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
G488V
-
clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
P409R
-
natural occurring point mutation, reconstructed by site-directed mutagenesis, the gene g6pd is highly polymorphic with over 130 mutations identified, reduced activity drastically altered kinetics, and altered tertiary structure, disturbing the binding of NADP+, compared to the wild-type enzyme, reduced thermal stbility
P489S
-
missense mutation associated with severe enzyme deficiency
R393E
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is slightly reduced compared to the activity of the wild-type enzyme
R393I
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393L
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393V
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is reduced compared to the activity of the wild-type enzyme
R454C
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Union clone, C1360T, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
R454H
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Andalus clone, G1361A, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
additional information